Literature summary for 4.2.2.3 extracted from

Svanem, B.I.; Strand, W.I.; Ertesvag, H.; Skjak-Braek, G.; Hartmann, M.; Barbeyron, T.; Valla, S.
The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme (2001), J. Biol. Chem., 276, 31542-31550.

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	the lyase activity is probably stimulated by the epimerase activity forming more guluronate residues at the reducing end of the substrate polymers	Azotobacter vinelandii

Cloned(Commentary)

Cloned (Comment)	Organism
gene algE1-1	Azotobacter vinelandii

Protein Variants

Protein Variants	Comment	Organism
D152G	nearly inactive mutant	Azotobacter vinelandii
D152G	mutation eliminates almost all of both the lyase and epimerase activities	Azotobacter vinelandii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics	Azotobacter vinelandii

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	secretion	Azotobacter vinelandii	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	dependent on	Azotobacter vinelandii

Organism

Organism	UniProt	Comment	Textmining
Azotobacter vinelandii	-	bifunctional enzyme comprising alginate lyase activity as well as mannuronan C-5-epimerase activity	-
Azotobacter vinelandii	Q9ZFG9	bifunctional mannuronan C-5-epimerase and alginate lyase, reaction of EC 5.1.3.37	-

Reaction

Reaction	Comment	Organism	Reaction ID
R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	alginate lyase activity and mannuronan C-5-epimerase activity of the bifunctional enzyme might use the same active site	Azotobacter vinelandii	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
culture medium	-	Azotobacter vinelandii	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alginate	isoform AlgE7 degrades M-rich alginates and a relatively G-rich alginate from the brown algae Macrocystis pyrifera most effectively, producing oligomers of 4 (mannuronan) to 7 units. The sequences cleaved are mainly G-MM and/or G-GM. G-moieties dominate at the reducing ends even when mannuronan is used as substrate, so the AlgE7 lyase/epimerase probably stimulates the lyase pathway, indicating a complex interplay between the two activities	Azotobacter vinelandii	oligouronides	-	?
alginate	substrate from brown algae Macrocystis pyrifera rich in polymannuronate and polyguluronate, cleavage sequences are G-/-MM and/or G-/-GM	Azotobacter vinelandii	oligosaccharides of 4-7 monomers	-	?
additional information	substrate specificity	Azotobacter vinelandii	?	-	?

Synonyms

Synonyms	Comment	Organism
AlgE7	-	Azotobacter vinelandii
alginate lyase	-	Azotobacter vinelandii
More	enzyme belongs to the family of secreted Ca2+-dependent epimerases	Azotobacter vinelandii

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Release 2023.1 (January 2023)